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Methyl-CpG-binding domain protein 3 (Methyl-CpG-binding protein MBD3)

 MBD3_HUMAN              Reviewed;         291 AA.
O95983; A8K4B7; D6W5Z2; Q6PIL9; Q6PJZ9; Q86XF4;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 149.
RecName: Full=Methyl-CpG-binding domain protein 3;
AltName: Full=Methyl-CpG-binding protein MBD3;
Name=MBD3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9774669; DOI=10.1128/MCB.18.11.6538;
Hendrich B., Bird A.;
"Identification and characterization of a family of mammalian methyl-
CpG binding proteins.";
Mol. Cell. Biol. 18:6538-6547(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, Cervix, Muscle, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, HETERODIMERIZATION WITH MBD2, AND INTERACTION WITH DNMT1.
PubMed=10947852; DOI=10.1046/j.1365-2443.2000.00359.x;
Tatematsu K., Yamazaki T., Ishikawa F.;
"MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex
containing DNMT1 at the replication foci in late S phase.";
Genes Cells 5:677-688(2000).
[7]
INTERACTION WITH THE HDAC1 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11102443; DOI=10.1074/jbc.M007372200;
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
Howard B.H.;
"Stable histone deacetylase complexes distinguished by the presence of
SANT domain proteins CoREST/kiaa0071 and Mta-L1.";
J. Biol. Chem. 276:6817-6824(2001).
[8]
FUNCTION, INTERACTION WITH HDAC1; MTA2 AND THE NURD COMPLEX, AND
MUTAGENESIS OF HIS-30 AND PHE-34.
PubMed=12124384; DOI=10.1074/jbc.M203455200;
Saito M., Ishikawa F.;
"The mCpG-binding domain of human MBD3 does not bind to mCpG but
interacts with NuRD/Mi2 components HDAC1 and MTA2.";
J. Biol. Chem. 277:35434-35439(2002).
[9]
INTERACTION WITH P66ALPHA AND P66BETA.
PubMed=12183469; DOI=10.1074/jbc.M207467200;
Brackertz M., Boeke J., Zhang R., Renkawitz R.;
"Two highly related p66 proteins comprise a new family of potent
transcriptional repressors interacting with MBD2 and MBD3.";
J. Biol. Chem. 277:40958-40966(2002).
[10]
INTERACTION WITH P66BETA AND THE MECP1 COMPLEX.
PubMed=11756549; DOI=10.1128/MCB.22.2.536-546.2002;
Feng Q., Cao R., Xia L., Erdjument-Bromage H., Tempst P., Zhang Y.;
"Identification and functional characterization of the p66/p68
components of the MeCP1 complex.";
Mol. Cell. Biol. 22:536-546(2002).
[11]
INTERACTION WITH BCL6, AND IDENTIFICATION IN THE NURD COMPLEX.
PubMed=15454082; DOI=10.1016/j.cell.2004.09.014;
Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R.,
Boss J.M., Wade P.A.;
"MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte
differentiation.";
Cell 119:75-86(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
FUNCTION.
PubMed=18644863; DOI=10.1128/MCB.00467-08;
Morey L., Brenner C., Fazi F., Villa R., Gutierrez A., Buschbeck M.,
Nervi C., Minucci S., Fuks F., Di Croce L.;
"MBD3, a component of the NuRD complex, facilitates chromatin
alteration and deposition of epigenetic marks.";
Mol. Cell. Biol. 28:5912-5923(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-144, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-85 AND SER-144,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-85, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-85, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23361464; DOI=10.1093/nar/gkt035;
Gunther K., Rust M., Leers J., Boettger T., Scharfe M., Jarek M.,
Bartkuhn M., Renkawitz R.;
"Differential roles for MBD2 and MBD3 at methylated CpG islands,
active promoters and binding to exon sequences.";
Nucleic Acids Res. 41:3010-3021(2013).
[22]
SUBCELLULAR LOCATION.
PubMed=24385926; DOI=10.1371/journal.pgen.1004028;
Shimbo T., Du Y., Grimm S.A., Dhasarathy A., Mav D., Shah R.R.,
Shi H., Wade P.A.;
"MBD3 localizes at promoters, gene bodies and enhancers of active
genes.";
PLoS Genet. 9:E1004028-E1004028(2013).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-90 AND LYS-92, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[24]
STRUCTURE BY NMR OF 1-70, FUNCTION, DNA-BINDING, AND MUTAGENESIS OF
HIS-30 AND PHE-34.
PubMed=24307175; DOI=10.1074/jbc.M113.512236;
Cramer J.M., Scarsdale J.N., Walavalkar N.M., Buchwald W.A.,
Ginder G.D., Williams D.C. Jr.;
"Probing the dynamic distribution of bound states for methylcytosine-
binding domains on DNA.";
J. Biol. Chem. 289:1294-1302(2014).
-!- FUNCTION: Acts as transcriptional repressor and plays a role in
gene silencing. Does not bind to DNA by itself (PubMed:12124384).
Binds to DNA with a preference for sites containing methylated CpG
dinucleotides (in vitro). Binds to a lesser degree DNA containing
unmethylated CpG dinucleotides (PubMed:24307175). Recruits histone
deacetylases and DNA methyltransferases.
{ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12124384,
ECO:0000269|PubMed:18644863, ECO:0000269|PubMed:23361464,
ECO:0000269|PubMed:24307175, ECO:0000269|PubMed:9774669}.
-!- SUBUNIT: Heterodimer with MBD2. Part of the NuRD and the MeCP1
complex. Interacts with BCL6, HDAC1, MTA2, DNMT1, p66-alpha and
p66-beta. {ECO:0000269|PubMed:10947852,
ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:11756549,
ECO:0000269|PubMed:12124384, ECO:0000269|PubMed:12183469,
ECO:0000269|PubMed:15454082}.
-!- INTERACTION:
Q8TAP6:CEP76; NbExp=4; IntAct=EBI-11978579, EBI-742887;
P17844:DDX5; NbExp=4; IntAct=EBI-1783068, EBI-351962;
Q8WXI9:GATAD2B; NbExp=4; IntAct=EBI-1783068, EBI-923440;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-1783068, EBI-618309;
Q13547:HDAC1; NbExp=6; IntAct=EBI-1783068, EBI-301834;
Q05084:ICA1; NbExp=3; IntAct=EBI-1783068, EBI-1046751;
O60341:KDM1A; NbExp=4; IntAct=EBI-1783068, EBI-710124;
O43474:KLF4; NbExp=3; IntAct=EBI-1783068, EBI-7232405;
P19012:KRT15; NbExp=3; IntAct=EBI-1783068, EBI-739566;
P43356:MAGEA2B; NbExp=4; IntAct=EBI-11978579, EBI-5650739;
P01106:MYC; NbExp=3; IntAct=EBI-1783068, EBI-447544;
Q01860:POU5F1; NbExp=3; IntAct=EBI-1783068, EBI-475687;
Q96D15:RCN3; NbExp=3; IntAct=EBI-1783068, EBI-746283;
O00560:SDCBP; NbExp=3; IntAct=EBI-1783068, EBI-727004;
P48431:SOX2; NbExp=3; IntAct=EBI-1783068, EBI-6124081;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-1783068, EBI-2130429;
Q8WWA6:ZNF277; NbExp=3; IntAct=EBI-1783068, EBI-10192794;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Nuclear, in
discrete foci. Detected on chromatin, at promoter regions of
active genes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95983-1; Sequence=Displayed;
Name=2;
IsoId=O95983-2; Sequence=VSP_011081;
Note=No experimental confirmation available.;
-!- SEQUENCE CAUTION:
Sequence=AAH32443.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF072247; AAC68876.1; -; mRNA.
EMBL; AK290882; BAF83571.1; -; mRNA.
EMBL; AC005943; AAC72104.1; -; Genomic_DNA.
EMBL; CH471139; EAW69477.1; -; Genomic_DNA.
EMBL; CH471139; EAW69478.1; -; Genomic_DNA.
EMBL; CH471139; EAW69481.1; -; Genomic_DNA.
EMBL; BC009372; AAH09372.1; -; mRNA.
EMBL; BC009438; AAH09438.1; -; mRNA.
EMBL; BC032443; AAH32443.1; ALT_INIT; mRNA.
EMBL; BC043619; AAH43619.1; -; mRNA.
CCDS; CCDS12072.1; -. [O95983-1]
CCDS; CCDS62481.1; -. [O95983-2]
RefSeq; NP_001268382.1; NM_001281453.1. [O95983-1]
RefSeq; NP_001268383.1; NM_001281454.1. [O95983-2]
UniGene; Hs.178728; -.
UniGene; Hs.595754; -.
PDB; 2MB7; NMR; -; A=1-70.
PDBsum; 2MB7; -.
ProteinModelPortal; O95983; -.
SMR; O95983; -.
BioGrid; 119788; 89.
CORUM; O95983; -.
DIP; DIP-46517N; -.
IntAct; O95983; 76.
MINT; MINT-4822095; -.
STRING; 9606.ENSP00000156825; -.
iPTMnet; O95983; -.
PhosphoSitePlus; O95983; -.
EPD; O95983; -.
MaxQB; O95983; -.
PaxDb; O95983; -.
PeptideAtlas; O95983; -.
PRIDE; O95983; -.
DNASU; 53615; -.
Ensembl; ENST00000156825; ENSP00000156825; ENSG00000071655. [O95983-2]
Ensembl; ENST00000434436; ENSP00000412302; ENSG00000071655. [O95983-1]
GeneID; 53615; -.
KEGG; hsa:53615; -.
UCSC; uc002ltj.5; human. [O95983-1]
CTD; 53615; -.
DisGeNET; 53615; -.
EuPathDB; HostDB:ENSG00000071655.17; -.
GeneCards; MBD3; -.
H-InvDB; HIX0014590; -.
HGNC; HGNC:6918; MBD3.
HPA; CAB013265; -.
MIM; 603573; gene.
neXtProt; NX_O95983; -.
OpenTargets; ENSG00000071655; -.
PharmGKB; PA30661; -.
eggNOG; ENOG410INB5; Eukaryota.
eggNOG; ENOG410XSPC; LUCA.
GeneTree; ENSGT00410000025376; -.
HOGENOM; HOG000013073; -.
HOVERGEN; HBG052417; -.
InParanoid; O95983; -.
KO; K11591; -.
OMA; LMHAVII; -.
OrthoDB; EOG091G0I05; -.
PhylomeDB; O95983; -.
TreeFam; TF325032; -.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SIGNOR; O95983; -.
ChiTaRS; MBD3; human.
GeneWiki; MBD3; -.
GenomeRNAi; 53615; -.
PRO; PR:O95983; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000071655; -.
CleanEx; HS_MBD3; -.
ExpressionAtlas; O95983; baseline and differential.
Genevisible; O95983; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0016581; C:NuRD complex; NAS:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0016573; P:histone acetylation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0006346; P:methylation-dependent chromatin silencing; IBA:GO_Central.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0009888; P:tissue development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR032343; MBD2/MBD3_p55-bd.
InterPro; IPR025884; MeCpG-bd_2/3_C_dom.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
Pfam; PF01429; MBD; 1.
Pfam; PF14048; MBD_C; 1.
Pfam; PF16564; MBDa; 1.
SMART; SM00391; MBD; 1.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Coiled coil;
Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 291 Methyl-CpG-binding domain protein 3.
/FTId=PRO_0000096262.
DOMAIN 1 72 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
COILED 216 245 {ECO:0000255}.
COMPBIAS 272 281 Poly-Glu.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 90 90 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 5 36 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011081.
MUTAGEN 30 30 H->K: No effect. Confers strong binding
to methylated CpG (in vitro); when
associated with Y-34.
{ECO:0000269|PubMed:12124384,
ECO:0000269|PubMed:24307175}.
MUTAGEN 34 34 F->A: Augments DNA binding activity,
irrespective of DNA methylation.
{ECO:0000269|PubMed:12124384,
ECO:0000269|PubMed:24307175}.
MUTAGEN 34 34 F->Y: Confers weak binding to methylated
CpG (in vitro). Confers strong binding to
methylated CpG (in vitro); when
associated with K-30.
{ECO:0000269|PubMed:12124384,
ECO:0000269|PubMed:24307175}.
STRAND 16 24 {ECO:0000244|PDB:2MB7}.
STRAND 27 36 {ECO:0000244|PDB:2MB7}.
HELIX 46 53 {ECO:0000244|PDB:2MB7}.
TURN 54 56 {ECO:0000244|PDB:2MB7}.
TURN 64 67 {ECO:0000244|PDB:2MB7}.
SEQUENCE 291 AA; 32844 MW; B62134DD1BEB636B CRC64;
MERKRWECPA LPQGWEREEV PRRSGLSAGH RDVFYYSPSG KKFRSKPQLA RYLGGSMDLS
TFDFRTGKML MSKMNKSRQR VRYDSSNQVK GKPDLNTALP VRQTASIFKQ PVTKITNHPS
NKVKSDPQKA VDQPRQLFWE KKLSGLNAFD IAEELVKTMD LPKGLQGVGP GCTDETLLSA
IASALHTSTM PITGQLSAAV EKNPGVWLNT TQPLCKAFMV TDEDIRKQEE LVQQVRKRLE
EALMADMLAH VEELARDGEA PLDKACAEDD DEEDEEEEEE EPDPDPEMEH V


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